8cmc

Human Leukocyte Antigen class II allotype DR1 presenting SARS-CoV-2 Spike peptide S511-530

Method: X-RAY DIFFRACTION Dmax: 84.1 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

HLA class II histocompatibility antigen, DR alpha chain

Homo sapiens

UniProt P01903

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 26–207 Not recorded Human leukocyte antigen DR beta chain allotype DR1 (DRB1*0101) × 1 ;Spike protein S2' ; × 1 (P0DTC2) EDO 1,2-ETHANEDIOL × 15 SO4 SULFATE ION × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;291 K;0.1 M MES pH 7.0, 25 % PEG8000, 0.2 M (NH4)2SO4 Resolution 1.42 Å R-free 0.208

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

139 other PDB entries and 219 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DRA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–183; UniProt 26–207

;Spike protein S2' ;

OrganismNot specified

UniProt P0DTC2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 511–530 Not recorded HLA class II histocompatibility antigen, DR alpha chain × 1 (P01903) Human leukocyte antigen DR beta chain allotype DR1 (DRB1*0101) × 1 EDO 1,2-ETHANEDIOL × 15 SO4 SULFATE ION × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;291 K;0.1 M MES pH 7.0, 25 % PEG8000, 0.2 M (NH4)2SO4 Resolution 1.42 Å R-free 0.208

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

2152 other PDB entries and 2473 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPIKE_SARS2
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–20; UniProt 511–530

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8cmc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8cmc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8cmc
Deposition date deposition_date2023-02-19
Structure title titleHuman Leukocyte Antigen class II allotype DR1 presenting SARS-CoV-2 Spike peptide S511-530
Keywords keywords;HLA-II, HLA-DR, HLA-DR1, human leukocyte antigen, major histocompatibility complex, major histocompatibility complex class 2, SARS-CoV-2, coronavirus, COVID-19, Spike, IMMUNE SYSTEM ;; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier24.83
Radius of gyration Rg (electron density) rg_electron23.87
Forward intensity I(0) i036124600.00
Molecular weight molecular_weight46188.0 kDa
Excluded volume excluded_volume57648 ų
Envelope volume envelope_volume69569 ų
Hydration-shell volume shell_volume24769 ų
Envelope diameter envelope_diameter86.4
Shell Rg shell_rg30.38
Envelope Rg envelope_rg24.13
Shape Rg shape_rg23.83
Total Rg total_rg24.72
Total atoms total_atoms3253
Residues n_residues388
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax84.1
Rg (real space) rg_real24.86
Rg uncertainty (real space) rg_real_error0.73
I(0) (real space) i0_real3.6120e+07
I(0) uncertainty (real space) i0_real_error5.2960e+05
Rg (reciprocal space) rg_reciprocal24.85
I(0) (reciprocal space) i0_reciprocal36120000.0000
Solution quality estimate total_estimate0.8040
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.0
Skewness Skewness skewness0.371
Kurtosis Kurtosis kurtosis-0.347
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9010000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.842; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.930; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)